Hofhuis, Julia

[["dc.bibliographiccitation.firstpage","362"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Structural Biology"],["dc.bibliographiccitation.lastpage","371"],["dc.bibliographiccitation.volume","175"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Hofhuis, Julia"],["dc.contributor.author","Thoeing, Christian"],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Niemann, Hartmut H."],["dc.date.accessioned","2017-09-07T11:43:25Z"],["dc.date.available","2017-09-07T11:43:25Z"],["dc.date.issued","2011"],["dc.description.abstract","The yeast peroxisomal hydrolase Lpx1 belongs to the alpha/beta-hydrolase superfamily. In the absence of Lpx1, yeast peroxisomes show an aberrant vacuolated morphology similar to what is found in peroxisomal disorder patients. Here, we present the crystal structure of Lpx1 determined at a resolution of 1.9 angstrom. The structure reveals the complete catalytic triad with an unusual location of the acid residue after strand beta 6 of the canonical alpha/beta-hydrolase fold. A four-helix cap domain covers the active site. The interface between the alpha/beta-hydrolase core and the cap domain forms the potential substrate binding site, which may also comprise the tunnel that leads into the protein interior and widens into a cavity. Two further tunnels connect the active site to the protein surface, potentially facilitating substrate access. Lpx1 is a homodimer. The alpha/beta-hydrolase core folds of the two protomers form the dimer contact site. Further dimerization contacts arise from the mutual embracement of the cap domain of one protomer by the non-canonical C-terminal helix of the other, resulting in a total buried surface area of some 6000 angstrom(2). The unusual C-terminal helix sticks out from the core fold to which it is connected by an extended flexible loop. We analyzed whether this helix is required for dimerization and for import of the dimer into peroxisomes using biochemical assays in vitro and a microscopy-based interaction assay in mammalian cells. Surprisingly, the C-terminal helix is dispensable for dimerization and dimer import. The unusually robust self-interaction suggests that Lpx1 is imported into peroxisomes as dimer. (C) 2011 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.jsb.2011.06.008"],["dc.identifier.gro","3142679"],["dc.identifier.isi","000293807000012"],["dc.identifier.pmid","21741480"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/109"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1047-8477"],["dc.title","The unusual extended C-terminal helix of the peroxisomal alpha/beta-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"],["local.message.claim","2020-08-07T08:23:16.626+0000|||rp114519|||submit_approve|||dc_contributor_author|||None"]]

[["dc.bibliographiccitation.firstpage","1119"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Europace"],["dc.bibliographiccitation.lastpage","1131"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Hofhuis, Julia"],["dc.contributor.author","Bersch, Kristina"],["dc.contributor.author","Wagner, Stefan"],["dc.contributor.author","Molina, Cristina Espinosa"],["dc.contributor.author","Fakuade, Funsho E."],["dc.contributor.author","Iyer, Lavanya M."],["dc.contributor.author","Streckfuß-Bömeke, Katrin"],["dc.contributor.author","Toischer, Karl"],["dc.contributor.author","Zelarayan, Laura Cecilia"],["dc.contributor.author","Voigt, Niels"],["dc.contributor.author","Nikolaev, Viacheslav O."],["dc.contributor.author","Maier, Lars Siegfried"],["dc.contributor.author","Klinge, Lars"],["dc.contributor.author","Thoms, Sven"],["dc.date.accessioned","2020-08-10T05:34:04Z"],["dc.date.available","2020-08-10T05:34:04Z"],["dc.date.issued","2020"],["dc.description.abstract","The multi-C2 domain protein dysferlin localizes to the T-Tubule system of skeletal and heart muscles. In skeletal muscle, dysferlin is known to play a role in membrane repair and in T-tubule biogenesis and maintenance. Dysferlin deficiency manifests as muscular dystrophy of proximal and distal muscles. Cardiomyopathies have been also reported, and some dysferlinopathy mouse models develop cardiac dysfunction under stress. Generally, the role and functional relevance of dysferlin in the heart is not clear. The aim of this study was to analyse the effect of dysferlin deficiency on the transverse-axial tubule system (TATS) structure and on Ca2+ homeostasis in the heart."],["dc.identifier.doi","10.1093/europace/euaa093"],["dc.identifier.pmid","32572487"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/67547"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/360"],["dc.language.iso","en"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A10: Peroxisomen als modulatorische Einheiten im Herzstoffwechsel und bei Herzinsuffizienz"],["dc.relation","SFB 1002 | C07: Kardiomyozyten Wnt/β-catenin Komplex Aktivität im pathologischen Herz-Remodeling - als gewebespezifischer therapeutischer Ansatz"],["dc.relation","SFB 1002 | D04: Bedeutung der Methylierung von RNA (m6A) und des Histons H3 (H3K4) in der Herzinsuffizienz"],["dc.relation","SFB 1002 | S01: In vivo und in vitro Krankheitsmodelle"],["dc.relation","SFB 1002 | A13: Bedeutung einer gestörten zytosolischen Calciumpufferung bei der atrialen Arrhythmogenese bei Patienten mit Herzinsuffizienz (HF)"],["dc.relation.eissn","1532-2092"],["dc.relation.issn","1099-5129"],["dc.relation.workinggroup","RG L. Maier (Experimentelle Kardiologie)"],["dc.relation.workinggroup","RG Nikolaev (Cardiovascular Research Center)"],["dc.relation.workinggroup","RG Thoms (Biochemistry and Molecular Medicine)"],["dc.relation.workinggroup","RG Toischer (Kardiales Remodeling)"],["dc.relation.workinggroup","RG Voigt (Molecular Pharmacology)"],["dc.relation.workinggroup","RG Zelarayán-Behrend (Developmental Pharmacology)"],["dc.title","Dysferlin links excitation-contraction coupling to structure and maintenance of the cardiac transverse-axial tubule system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","81"],["dc.bibliographiccitation.lastpage","92"],["dc.bibliographiccitation.seriesnr","1595"],["dc.contributor.author","Hofhuis, Julia"],["dc.contributor.author","Dieterle, Severin"],["dc.contributor.author","George, Rosemol"],["dc.contributor.author","Schueren, Fabian"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.editor","Schrader, M."],["dc.date.accessioned","2018-10-08T09:34:19Z"],["dc.date.available","2018-10-08T09:34:19Z"],["dc.date.issued","2017"],["dc.description.abstract","Translational readthrough, the decoding of stop codons as sense codons, leads to C-terminal extension of proteins which may lead to the formation of protein isoforms with distinct properties from the original protein. Two proteins have recently been identified that are targeted to the peroxisome via hidden peroxisomal targeting signals in their readthrough extensions. This noninduced basal translational readthrough can be distinguished from pharmacological induction of readthrough by aminoglycosides or other small molecules, which can be used for the treatment of diseases caused by premature stop (termination) codons (PTCs). Readthrough of both, natural stop codons and PTCs, can be quantified in cell culture using reporter systems. In the present article, we describe two dual reporter systems, based on combined fluorescence/luminescence measurement and flow cytometric fluorescence measurement, respectively. Further, we provide a protocol for a fast and efficient cloning procedure of reporter constructs. The dual reporter systems described here help to analyze the peroxisome-specific isoforms of readthrough enzymes as well as potential readthrough therapeutics."],["dc.fs.pkfprnr","54350"],["dc.identifier.doi","10.1007/978-1-4939-6937-1_9"],["dc.identifier.fs","632465"],["dc.identifier.pmid","28409454"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15877"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.publisher","Humana Press"],["dc.publisher.place","New York"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.eisbn","978-1-4939-6937-1"],["dc.relation.isbn","978-1-4939-6935-7"],["dc.relation.ispartof","Peroxisomes"],["dc.relation.ispartofseries","Methods in Molecular Biology;1595"],["dc.title","Dual Reporter Systems for the Analysis of Translational Readthrough in Mammals"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"],["local.message.claim","2020-08-07T08:23:16.626+0000|||rp114519|||submit_approve|||dc_contributor_author|||None"]]

[["dc.bibliographiccitation.firstpage","841"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","852"],["dc.bibliographiccitation.volume","130"],["dc.contributor.author","Hofhuis, Julia"],["dc.contributor.author","Bersch, Kristina"],["dc.contributor.author","Büssenschütt, Ronja"],["dc.contributor.author","Drzymalski, Marzena"],["dc.contributor.author","Liebetanz, David"],["dc.contributor.author","Nikolaev, Viacheslav O."],["dc.contributor.author","Wagner, Stefan"],["dc.contributor.author","Maier, Lars S."],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Klinge, Lars"],["dc.contributor.author","Thoms, Sven"],["dc.date.accessioned","2018-04-23T11:47:27Z"],["dc.date.available","2018-04-23T11:47:27Z"],["dc.date.issued","2017"],["dc.description.abstract","The multi-C2 domain protein dysferlin localizes to the plasma membrane and the T-tubule system in skeletal muscle; however, its physiological mode of action is unknown. Mutations in the DYSF gene lead to autosomal recessive limb-girdle muscular dystrophy type 2B and Miyoshi myopathy. Here, we show that dysferlin has membrane tubulating capacity and that it shapes the T-tubule system. Dysferlin tubulates liposomes, generates a T-tubule-like membrane system in non-muscle cells, and links the recruitment of phosphatidylinositol 4,5-bisphosphate to the biogenesis of the T-tubule system. Pathogenic mutant forms interfere with all of these functions, indicating that muscular wasting and dystrophy are caused by the dysferlin mutants' inability to form a functional T-tubule membrane system."],["dc.identifier.doi","10.1242/jcs.198861"],["dc.identifier.gro","3142220"],["dc.identifier.pmid","28104817"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13342"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/160"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A10: Peroxisomen als modulatorische Einheiten im Herzstoffwechsel und bei Herzinsuffizienz"],["dc.relation.issn","0021-9533"],["dc.relation.workinggroup","RG L. Maier (Experimentelle Kardiologie)"],["dc.relation.workinggroup","RG Nikolaev (Cardiovascular Research Center)"],["dc.relation.workinggroup","RG Thoms (Biochemistry and Molecular Medicine)"],["dc.title","Dysferlin mediates membrane tubulation and links T-tubule biogenesis to muscular dystrophy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"],["local.message.claim","2020-08-07T08:23:16.626+0000|||rp114519|||submit_approve|||dc_contributor_author|||None"]]

[["dc.bibliographiccitation.issue","9-10"],["dc.bibliographiccitation.journal","Neuromuscular Disorders"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Hofhuis, Julia"],["dc.contributor.author","Thoms, Sven"],["dc.contributor.author","Klinge, Lars"],["dc.date.accessioned","2018-11-07T09:34:36Z"],["dc.date.available","2018-11-07T09:34:36Z"],["dc.date.issued","2014"],["dc.identifier.doi","10.1016/j.nmd.2014.06.361"],["dc.identifier.isi","000342870200358"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32205"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.publisher.place","Oxford"],["dc.relation.eventlocation","Berlin, GERMANY"],["dc.title","Membrane and phospholipid binding properties of dysferlin"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]